Mass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis.

Abstract

Adhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted β1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and α5 and β1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.

• Authors: Manohar C Dange, Hemangi S Bhonsle, Rashmi K Godbole, Shyam K More, Sanjay M Bane, Mahesh J Kulkarni, Rajiv D Kalraiya
• Journal: Molecular bioSystems (Mol Biosyst) Vol. 13 Issue 11 Pg. 2303-2309 (Oct 24 2017) ISSN: 1742-2051 [Electronic] England
• PMID: 28875213 (Publication Type: Journal Article)

Chemical References

• Carrier Proteins
• Galectin 3

Topics

• Animals
• Carrier Proteins (metabolism)
• Chromatography, Affinity
• Chromatography, Liquid
• Galectin 3 (metabolism)
• Lung Neoplasms (metabolism, secondary)
• Mass Spectrometry (methods)
• Melanoma (pathology)
• Melanoma, Experimental
• Mice
• Protein Binding
• Protein Interaction Mapping (methods)
• Reproducibility of Results
• Workflow